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Perspectives
Dynamic Regulation of Effector Protein Binding to Histone Modifications: The Biology of HP1 Switching
Holger L. Dormann, Boo Shan Tseng, C. David Allis, Hironori Funabiki and Wolfgang Fischle
volume 5 | issue 24
15 december 2006Pages: 2842 - 2851
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Post-translational modifications of histone proteins, the basic building blocks around which eukaryotic DNA is organized, are crucially involved in the regulation of genome activity as they control chromatin structure and dynamics. The recruitment of specific binding proteins that recognize and interact with particular histone modifications is thought to constitute a fundamental mechanism by which histone marks mediate biological function. For instance, tri-methylation of histone H3 lysine 9 (H3K9me3) is important for recruiting heterochromatin protein 1 (HP1) to discrete regions of the genome, thereby regulating gene expression, chromatin packaging, and heterochromatin formation. Until now, little was known about the regulation of effector-histone mark interactions, and in particular, of the binding of HP1 to H3K9me3. Recently, we and others presented evidence that a "binary methylation-phosphorylation switch" mechanism controls the dynamic release of HP1 from H3K9me3 during the cell cycle: phosphorylation of histone H3 serine 10 (H3S10ph) occurs at the onset of mitosis, interferes with HP1-H3K9me3 interaction, and therefore, ejects HP1 from its binding site. Here, we discuss the biological function of HP1 release from chromatin during mitosis, consider implications why the cell controls HP1 binding by such a methylation-phosphorylation switching mechanism, and reflect on other cellular pathways where binary switching of HP1 might occur.
Authors
Holger L. Dormann
The Rockefeller University, New York, NY
Boo Shan Tseng
The Rockefeller University, New York, NY
C. David Allis
The Rockefeller University, New York, NY
Hironori Funabiki
The Rockefeller University, New York, NY
Wolfgang Fischle
Max-Planck Institute for Biophysical Chemistry; Göttingen, Germany
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.